ID   GSH1_ALIFM              Reviewed;         521 AA.
AC   B5FAD9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE            Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN   Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578}; OrderedLocusNames=VFMJ11_0555;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00578}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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DR   EMBL; CP001139; ACH65188.1; -; Genomic_DNA.
DR   RefSeq; WP_012532880.1; NC_011184.1.
DR   AlphaFoldDB; B5FAD9; -.
DR   SMR; B5FAD9; -.
DR   PRIDE; B5FAD9; -.
DR   EnsemblBacteria; ACH65188; ACH65188; VFMJ11_0555.
DR   KEGG; vfm:VFMJ11_0555; -.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00578; Glu_cys_ligase; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   PANTHER; PTHR38761; PTHR38761; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT   CHAIN           1..521
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000129610"
SQ   SEQUENCE   521 AA;  59403 MW;  BC35982897C5B7A7 CRC64;
     MTEFINRLQK VASNPNAFKK TGRGIERETL RFTPGASLST KPHPEGVGSA LTHKYITTDF
     AESLLEFITP VSNDVDTVLK QLEDVHHYTV SHMGDEKLWP LSMPCFVTHD DDITLAQYGE
     SNVGKLKTTY REGLKRRYGS VMQVISGVHF NFSFSTEFWD ELFGEQSEDQ RKESVSDAYF
     ALIRNYYRFG WLIPYFFGAS PALCSSFIQG RETSMDFESL GKTYYLPYAT SLRLSDLGYT
     NDAQSNLKIS LNSVNEYVDG LNKAIRTPSE EFAKIGLKEG DKHIQLNSNV LQIENELYAP
     IRPKRVAKSG ERPSEALERD GVEYIEVRSL DVNPYSPIGV NEDQVRFLDM FLTWTVLSDS
     APMNDSEMAC WKDNWNKIIE KGRKPGLELK IGCQGERLTQ KAWAERVFED LLIIAKEMDR
     VNGDDAYQQT HKRLSAMIDD PELTISGRLL AETKAAGGIG VIGCKLAVEH RETHLAHQYR
     FYTKQELDTE VERSVQAQKE IEANDKLSFS EYLEEYFSYL K